Crystallization of the C-terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3

7Citations
Citations of this article
12Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Turkey adenovirus 3 belongs to the genus Siadenovirus. Its predicted fibre protein consists of an N-terminal virus-attachment domain, a central shaft domain and a head domain at the C-terminus. The head domain has little sequence identity to known adenovirus fibre head structures. Crystals of the fibre head domain consisting of amino acids 304-454 with an N-terminal purification tag were produced. Crystals of native and selenomethionine-derivatized protein belonged to space group I23 (unit-cell parameter 99 Å). They diffracted synchrotron radiation to 2.0 and 2.14 Å resolution, respectively, and are expected to contain one monomer in the asymmetric unit. © 2013 International Union of Crystallography All rights reserved.

Cite

CITATION STYLE

APA

Singh, A. K., Ballmann, M. Z., Benkö, M., Harrach, B., & Van Raaij, M. J. (2013). Crystallization of the C-terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(10), 1135–1139. https://doi.org/10.1107/S174430911302397X

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free